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Published online August 6, 2007
doi:10.1083/jcb.200612135
The Journal of Cell Biology, Vol. 178, No. 4, 557-565
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Sabri et al.
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Report

 Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport

Nafiseh Sabri, Peggy Roth, Nikos Xylourgidis, Fatemeh Sadeghifar, Jeremy Adler, and Christos Samakovlis

Department of Developmental Biology, Wenner-Gren Institute, Stockholm University, S-10691 Stockholm, Sweden

Correspondence to Christos Samakovlis: christos{at}devbio.su.se

The phenylanine-glycine (FG)–rich regions of several nucleoporins both bind to nuclear transport receptors and collectively provide a diffusion barrier to the nuclear pores. However, the in vivo roles of FG nucleoporins in transport remain unclear. We have inactivated 30 putative nucleoporins in cultured Drosophila melanogaster S2 cells by RNA interference and analyzed the phenotypes on importin {alpha}/ß–mediated import and CRM1-dependent protein export. The fly homologues of FG nucleoporins Nup358, Nup153, and Nup54 are selectively required for import. The FG repeats of Nup153 are necessary for its function in transport, whereas the remainder of the protein maintains pore integrity. Inactivation of the CRM1 cofactor RanBP3 decreased the nuclear accumulation of CRM1 and protein export. We report a surprisingly antagonistic relationship between RanBP3 and the Nup214 FG region in determining CRM1 localization and its function in protein export. Our data suggest that peripheral metazoan FG nucleoporins have distinct functions in nuclear protein transport events.

Abbreviations used in this paper: cNLS, classic NLS; dsRNA, double-stranded RNA; FG, phenylanine-glycine; NES, nuclear export signal; NPC, nuclear pore complex.


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